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|Type:||Artigo de periódico|
|Title:||Effects of lyophilization on catalytic properties of immobilized fructosyltransferase from Rhodotorula sp LEB-V10|
|Abstract:||The extracellular fructosyltransferase (FTase) from Rhodotorula sp. LEB-V10 was immobilized on particles of niobium-graphite alloy and freeze dried (lyophilized), with and without additives. Twelve additives commonly applied as cryoprotectants were selected and evaluated both individually and in formulation; the biocatalyst was then studied according to its catalytic properties. Lyophilization with or without additives did not significantly affect the immobilized enzyme. After a period of 6 months, reductions in the initial enzymatic activity of about 7 and 4% were observed for the lyophilized enzyme when using 50 and 200 mM sodium acetate buffers, respectively. CMC, sorbitol, inositol and trehalose as single additives (all at 2.5%, w/v) in 100 mM sodium acetate buffer were capable to preserve the enzymatic activity after 6 months. However, formulations with more than one additive resulted in 36-14% less enzymatic activity after 6 months. After lyophilization, FOS synthesis features changed positively, by increasing the FOS yield from a non-lyophilizated yield of 58-68% with lyophilization. FOS composition changed as well, with 1(F)-fructofuranosyl-nystose (GF(4)) content increasing to 61% with lyophilization, which is 76 times higher than with the non-lyophilized enzyme. (C) 2013 The Institution of Chemical Engineers. Published by Elsevier B.V. All rights reserved.|
|Editor:||Inst Chemical Engineers|
|Appears in Collections:||Unicamp - Artigos e Outros Documentos|
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